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Citations et références (20)
Invitrogen™
CMAC, t-BOC-Leu-Met (7-Amino-4-Chloromethylcoumarin, t-BOC-L-Leucyl-L-Methionine amide)
Le substrat de peptidase CMAC, t-BOC-Leu-Met, peut être utilisé pour mesurer l’activité de la peptidase dans une solution ou dansAfficher plus
| Référence | Quantité |
|---|---|
| A6520 | 5 mg |
Référence A6520
Prix (EUR)
492,00
Each
Quantité:
5 mg
Prix (EUR)
492,00
Each
Le substrat de peptidase CMAC, t-BOC-Leu-Met, peut être utilisé pour mesurer l’activité de la peptidase dans une solution ou dans les cellules vivantes. Le substrat possède des maxima d’excitation/d’émission ∼ 330/403. Après clivage par les peptidases, le produit génère une fluorescence bleue avec une excitation/émission maximales ∼ 351/430 nm.
Usage exclusivement réservé à la recherche. Ne pas utiliser pour des procédures de diagnostic.
Spécifications
Perméabilité cellulairePerméant aux cellules
Quantité5 mg
Conditions d’expéditionTempérature ambiante
SubstratSubstrat de peptidase CMAC
Méthode de détectionFluorescent
FormePleine
Substrate PropertiesSubstrat à base de peptides
Type de substratSubstrat de peptidase
Target EnzymeCalpain
Unit SizeEach
Contenu et stockage
Conserver au congélateur (-5 à -30 °C).
Citations et références (20)
Citations et références
Abstract
Calpain-mediated X-linked inhibitor of apoptosis degradation in neutrophil apoptosis and its impairment in chronic neutrophilic leukemia.
Journal:J Biol Chem
PubMed ID:12121983
'The number of neutrophils in the blood and tissues is controlled by constitutive apoptotic programmed cell death and clearance by phagocytes such as macrophages. Here, we found that calpains cleave the X-linked inhibitor of apoptosis (XIAP) in vitro, producing fragments that are unable to inhibit caspase-3. These fragments were detected
Suppression of cancer cell migration and invasion by protein phosphatase 2A through dephosphorylation of mu- and m-calpains.
Journal:J Biol Chem
PubMed ID:16982626
'The mu- and m-calpains are major members of the calpain family that play an essential role in regulating cell motility. We have recently discovered that nicotine-activated protein kinase C iota enhances calpain phosphorylation in association with enhanced calpain activity and accelerated migration and invasion of human lung cancer cells. Here
Protein kinase Ciota promotes nicotine-induced migration and invasion of cancer cells via phosphorylation of micro- and m-calpains.
Journal:J Biol Chem
PubMed ID:16361262
'Nicotine is a major component in cigarette smoke that activates the growth-promoting pathways to facilitate the development of lung cancer. However, it is not clear whether nicotine affects cell motility to facilitate tumor metastasis. Here we discovered that nicotine potently induces phosphorylation of both mu- and m-calpains via activation of
Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation.
Journal:J Biol Chem
PubMed ID:9873017
'The cytokine tumor necrosis factor alpha (TNF-alpha) induces expression of inflammatory gene networks by activating cytoplasmic to nuclear translocation of the nuclear factor-kappaB (NF-kappaB) transcription factor. NF-kappaB activation results from sequential phosphorylation and hydrolysis of the cytoplasmic inhibitor, IkappaBalpha, through the 26 S proteasome. Here, we show a parallel proteasome-independent
Calpain is required for normal osteoclast function and is down-regulated by calcitonin.
Journal:J Biol Chem
PubMed ID:16461769
'Osteoclast motility is thought to depend on rapid podosome assembly and disassembly. Both mu-calpain and m-calpain, which promote the formation and disassembly of focal adhesions, were observed in the podosome belt of osteoclasts. Calpain inhibitors disrupted the podosome belt, blocked the constitutive cleavage of the calpain substrates filamin A, talin,